SitesBLAST
Comparing AZOBR_RS05280 FitnessBrowser__azobra:AZOBR_RS05280 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
48% identity, 90% coverage: 11:219/232 of query aligns to 8:215/215 of P0AB87
- T26 (≠ S29) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- A27 (≠ S30) mutation Missing: Strong decrease of the aldolase activity.
- GN 28:29 (= GN 31:32) binding
- N29 (= N32) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
- TG 43:44 (≠ SS 46:47) binding
- S71 (= S74) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
- SS 71:72 (= SS 74:75) binding
- E73 (= E76) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
- H92 (= H95) binding
- H94 (= H97) binding
- Y113 (= Y116) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
- F131 (= F134) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
- H155 (= H158) binding
- F206 (≠ M208) mutation to W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
- 207:215 (vs. 209:219, 36% identical) mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
- Y209 (= Y213) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
- LRIEE 211:215 (≠ LPPDE 215:219) mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
49% identity, 86% coverage: 11:209/232 of query aligns to 8:207/210 of 2fuaA
Sites not aligning to the query:
1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
49% identity, 86% coverage: 11:209/232 of query aligns to 8:207/209 of 1dzuP
4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
49% identity, 85% coverage: 11:208/232 of query aligns to 8:206/206 of 4fuaA
- active site: E73 (= E76), H92 (= H95), H94 (= H97), Y113 (= Y116), A117 (≠ L120), H155 (= H158)
- binding phosphoglycolohydroxamic acid: G28 (= G31), N29 (= N32), T43 (≠ S46), S71 (= S74), S72 (= S75), E73 (= E76), H92 (= H95), H94 (= H97), H155 (= H158)
- binding zinc ion: H92 (= H95), H94 (= H97), H155 (= H158)
7x78A L-fuculose 1-phosphate aldolase (see paper)
48% identity, 85% coverage: 11:208/232 of query aligns to 8:203/203 of 7x78A
Sites not aligning to the query:
P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
39% identity, 87% coverage: 9:209/232 of query aligns to 6:208/213 of P0DTQ0
- E76 (= E76) binding
- H95 (= H95) binding
- H97 (= H97) binding
- H157 (= H158) binding
6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
39% identity, 86% coverage: 9:208/232 of query aligns to 6:207/207 of 6btgA
4c25A L-fuculose 1-phosphate aldolase (see paper)
44% identity, 80% coverage: 25:209/232 of query aligns to 25:211/212 of 4c25A
Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
27% identity, 75% coverage: 10:183/232 of query aligns to 3:169/181 of Q58813
- N25 (= N32) mutation to L: It shows a 3-fold increase of the affinty for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.
6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
29% identity, 75% coverage: 10:182/232 of query aligns to 8:185/207 of 6voqA
4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
28% identity, 74% coverage: 24:194/232 of query aligns to 37:208/249 of 4xxfA
P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 45% coverage: 10:113/232 of query aligns to 6:113/231 of P08203
- N28 (= N32) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- K42 (≠ T44) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
- D76 (≠ E76) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- H95 (= H95) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
- H97 (= H97) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
Sites not aligning to the query:
- 116 mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
- 120 D→N: Loss of the epimerase activity.
- 142 E→Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- 171 binding
- 218 H→N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
- 229 Y→F: Loss of the epimerase activity.
1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
31% identity, 45% coverage: 10:113/232 of query aligns to 6:113/223 of 1jdiA
Sites not aligning to the query:
Q988D0 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase; HMPDdc; EC 4.1.1.51 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see paper)
26% identity, 83% coverage: 10:201/232 of query aligns to 2:206/234 of Q988D0
- E73 (= E76) binding
- H92 (= H95) binding
- H94 (= H97) binding
- H163 (= H158) binding
2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
26% identity, 83% coverage: 10:201/232 of query aligns to 5:209/237 of 2z7bA
Query Sequence
>AZOBR_RS05280 FitnessBrowser__azobra:AZOBR_RS05280
MTSLSHPAQRRAIIDTCLAMNGAGINQGSSGNLSVRVEGGFLITPSSLPYDETAPEDIVE
MGFDGTYVGRRRPSSEWRFHRDILKARPDVDVVLHTHSTFATALAVHGRGIPSFHYMVAL
AGGDSIRCAPYATFGSQELSDHAVAALEGRLACLLANHGMIVLGKTPKGALALAVEVETL
ARQYLHAHLLGEPVILPPEEIARVAEKMRRMKYGLPPDEGAALEDTARPREA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory